The recombinant hemagglutinin of Influenza A virus (A/chicken/Italy/22A/ 1998(H5N9)) comprises 337 amino acids and has a predicted molecular mass of 38.1 kDa. The apparent molecular mass of the protein is approximately 48.5 kDa in SDS-PAGE under reducing conditions.

Formulation

Lyophilized from sterile PBS, pH 7.4.1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.2. Please contact us for any concerns or special requirements.

Please refer to the specific buffer information in the hard copy of CoA.

Shipping

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

Stability & Storage

Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Reconstitution

A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Hemagglutinin / HA Background Information

The influenza viral Hemagglutinin (HA) protein is a homo trimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of host endosomal membrane with the viral membrane.The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.